JKMRS Volume 25, No 1, pp 8, Backbone NMR chemical shift assig... | |
---|---|
2021년 03월 20일 / 조회수: 536 | |
Backbone NMR
chemical shift assignment of transthyretin Bokyung Kim and Jin Hae Kim* Department of New Biology, Daegu Gyeongbuk Institute of
Science and Technology, Daegu 42988, Republic of Korea Received Mar 19, 2021; Revised
Mar 19, 2021; Accepted Mar 19, 2021
Abstract Transthyretin
(TTR) is an important transporter protein for thyroxine (T4) and a
holo-retinol protein in human. In its native state, TTR forms a tetrameric
complex to construct the hydrophobic binding pocket for T4. On the
other hand, this protein is also infamous for its amyloidogenic propensity,
which causes various human diseases, such as senile systemic amyloidosis and
familial amyloid polyneuropathy/cardiomyopathy. In this work, to investigate
various structural features of TTR with solution-state nuclear magnetic
resonance (NMR) spectroscopy, we conducted backbone NMR signal assignments.
Except the N-terminal two residues and prolines, backbone 1H-15N
signals of all residues were successfully assigned with additional chemical
shift information of 13CO, 13Cα, and 13Cβ
for most residues. The chemical shift information reported here will become an
important basis for subsequent structural and functional studies of TTR.
Keywords transthyretin, transthyretin amyloidosis, NMR spectroscopy, chemical shift assignment
|
|
첨부파일 | 2_KimJH.pdf |